2CWY

Crystal structure of conserved hypothetical protein, TTHA0068 from Thermus thermophilus HB8

Experimental procedure

Experimental method	MAD
Source type	SYNCHROTRON
Source details	SPRING-8 BEAMLINE BL26B1
Synchrotron site	SPring-8
Beamline	BL26B1
Temperature [K]	100
Detector technology	CCD
Collection date	2005-05-27
Detector	RIGAKU JUPITER 210
Wavelength(s)	0.979148, 0.979457, 0.964
Spacegroup name	P 21 21 21
Unit cell lengths	36.232, 41.135, 54.034
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	32.730 - 1.850
R-factor	0.178
Rwork	0.178
R-free	0.21400
Structure solution method	MAD
RMSD bond length	0.007
RMSD bond angle	1.300
Data reduction software	HKL-2000
Data scaling software	SCALEPACK
Phasing software	SOLVE
Refinement software	CNS (1.1)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	50.000	1.920
High resolution limit [Å]	1.850	1.850
Number of reflections	7279
<I/σ(I)>	14.2	7.52
Completeness [%]	99.3	94.3
Redundancy	5.6

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	oil batch	7.5	293	PEG8000, Ethylene Glycol, pH 7.5, oil batch, temperature 293K